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RSGI4_ACET2
ID   RSGI4_ACET2             Reviewed;         522 AA.
AC   A3DCG3;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Anti-sigma-I factor RsgI4 {ECO:0000305};
GN   Name=rsgI4 {ECO:0000303|PubMed:20487018};
GN   OrderedLocusNames=Cthe_0404 {ECO:0000312|EMBL:ABN51642.1};
OS   Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS   103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=203119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC   B-4536 / VPI 7372;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA   Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NOMENCLATURE, AND DOMAIN.
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC   B-4536 / VPI 7372;
RX   PubMed=20487018; DOI=10.1111/j.1574-6968.2010.01997.x;
RA   Kahel-Raifer H., Jindou S., Bahari L., Nataf Y., Shoham Y., Bayer E.A.,
RA   Borovok I., Lamed R.;
RT   "The unique set of putative membrane-associated anti-sigma factors in
RT   Clostridium thermocellum suggests a novel extracellular carbohydrate-
RT   sensing mechanism involved in gene regulation.";
RL   FEMS Microbiol. Lett. 308:84-93(2010).
RN   [3]
RP   INDUCTION.
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC   B-4536 / VPI 7372;
RX   PubMed=24782837; DOI=10.3389/fmicb.2014.00142;
RA   Wei H., Fu Y., Magnusson L., Baker J.O., Maness P.C., Xu Q., Yang S.,
RA   Bowersox A., Bogorad I., Wang W., Tucker M.P., Himmel M.E., Ding S.Y.;
RT   "Comparison of transcriptional profiles of Clostridium thermocellum grown
RT   on cellobiose and pretreated yellow poplar using RNA-Seq.";
RL   Front. Microbiol. 5:142-142(2014).
RN   [4] {ECO:0007744|PDB:4B97}
RP   X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 374-522.
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC   B-4536 / VPI 7372;
RX   PubMed=24531486; DOI=10.1107/s139900471302926x;
RA   Yaniv O., Fichman G., Borovok I., Shoham Y., Bayer E.A., Lamed R.,
RA   Shimon L.J., Frolow F.;
RT   "Fine-structural variance of family 3 carbohydrate-binding modules as
RT   extracellular biomass-sensing components of Clostridium thermocellum anti-
RT   sigmaI factors.";
RL   Acta Crystallogr. D 70:522-534(2014).
CC   -!- FUNCTION: Anti-sigma factor for SigI4. Negatively regulates SigI4
CC       activity through direct interaction. Binding of the polysaccharide
CC       substrate to the extracellular C-terminal sensing domain of RsgI4 may
CC       induce a conformational change in its N-terminal cytoplasmic region,
CC       leading to the release and activation of SigI4.
CC       {ECO:0000250|UniProtKB:A3DBH1}.
CC   -!- SUBUNIT: Interacts (via RsgI N-terminal anti-sigma domain) with SigI4.
CC       {ECO:0000255|PROSITE-ProRule:PRU01196}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Up-regulated in pretreated yellow poplar (PYP)-grown cells.
CC       {ECO:0000269|PubMed:24782837}.
CC   -!- DOMAIN: The CBM3 domain binds to cellulose.
CC       {ECO:0000269|PubMed:20487018}.
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DR   EMBL; CP000568; ABN51642.1; -; Genomic_DNA.
DR   RefSeq; WP_003512704.1; NC_009012.1.
DR   PDB; 4B97; X-ray; 1.28 A; A=374-522.
DR   PDBsum; 4B97; -.
DR   AlphaFoldDB; A3DCG3; -.
DR   SMR; A3DCG3; -.
DR   STRING; 203119.Cthe_0404; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   EnsemblBacteria; ABN51642; ABN51642; Cthe_0404.
DR   KEGG; cth:Cthe_0404; -.
DR   eggNOG; COG4447; Bacteria.
DR   HOGENOM; CLU_511640_0_0_9; -.
DR   OMA; NTNGREM; -.
DR   OrthoDB; 989347at2; -.
DR   Proteomes; UP000002145; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.710; -; 1.
DR   InterPro; IPR024449; Anti-sigma_RsgI_N.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF12791; RsgI_N; 1.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   PROSITE; PS51172; CBM3; 1.
DR   PROSITE; PS51849; RSGI_N; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..522
FT                   /note="Anti-sigma-I factor RsgI4"
FT                   /id="PRO_0000436547"
FT   TOPO_DOM        1..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..522
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          2..49
FT                   /note="RsgI N-terminal anti-sigma"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01196"
FT   DOMAIN          371..522
FT                   /note="CBM3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   REGION          311..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  57828 MW;  5B869BD8C3FB63D3 CRC64;
     MNLGVVIKIK RKKAIIVTET GEFKAVNARN GMFLGQKILF DQQDVIENNR NGIGLAYSAA
     IAGMVAVFVF MFTYFGLHNF NGTFAYVDVD INPSVEFAVN RDGIVVNAEP LNDDGRKVLE
     ELIYKDALLE DVILDLVDKS RKYGFIEDND RKNIILISAA LNSDEQEQRN DFEKKLVDNL
     MPELENLDVN IEMRFVIASK EQRKKAQENK VSMGKYMIYE MARRQGEKLT LESIMSETLE
     NLLLGQDFGV IETEKTPVNT PVKSTATPTK ALAAEITPTK TPEQVVMTPA NTPAKPTAAP
     TKAPAAVAVT SAKTPERATT VPVNTPVKPT DAPTKSPATA TATATRAPVK ATATPAKTLK
     PSDTPVKTPD GEQSVKVRFY NNNTLSETGV IYMRINVINT GNAPLDLSDL KLRYYYTIDS
     ESEQRFNCDW SSIGAHNVTG SFGKVNPSRN GADTYVEIGF TKEAGMLQPG ESVELNARFS
     KTDNTQYNKA DDYSFNSHYY EYVDWDRITA YISGILKWGR EP
 
 
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